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Merck
CN

A method for detection of 4-hydroxy-2-nonenal adducts in proteins.

Free radical biology & medicine (2011-04-05)
Chika Wakita, Kazuya Honda, Takahiro Shibata, Mitsugu Akagawa, Koji Uchida
ABSTRACT

We developed a procedure to measure 4-hydroxy-2-nonenal (HNE)-amino acid adducts using the fluorescent probe 2-aminopyridine (2-AP). The method is based on the fact that HNE forms Michael addition-type amino acid adducts possessing an aldehyde functionality, which upon reaction with 2-AP in the presence of NaBH₃CN can be converted to their pyridylaminated derivatives. The HNE-amino acid adducts, namely Michael addition-type HNE-cysteine, HNE-histidine, and HNE-lysine adducts, after pyridylamination were resistant to conventional acid-hydrolysis conditions for protein (6N HCl/110°C/24 h) and could be detected by HPLC with a fluorescence detector. The reductive amination-based fluorescent labeling of HNE adducts is a simple and accurate technique that may be widely used to reveal increased levels of covalently modified proteins with HNE and its related aldehydes during aging and disease.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Sodium cyanoborohydride solution, 1.0 M in THF
Sigma-Aldrich
Sodium cyanoborohydride solution, 5.0 M in 1 M NaOH
Sigma-Aldrich
Sodium cyanoborohydride, reagent grade, 95%
Sigma-Aldrich
2-Aminopyridine, purum, ≥98.0% (NT)
Sigma-Aldrich
2-Aminopyridine, 99%
Sigma-Aldrich
2-Aminopyridine, ≥99%
Supelco
2-Aminopyridine, PESTANAL®, analytical standard